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Amyloid Fibrils

Amyloid Fibrils

Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining,...

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Updated: Sep 1, 2025

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Interactions with and Membrane Permeabilization of Brain Mitochondria by Amyloid Fibrils

Published on: September 28, 2019

α-Synuclein Interaction with Lipid Bilayer Discs.

Marija Dubackic¹, Yun Liu^2,3, Elizabeth G Kelley²

¹Physical Chemistry, Department of Chemistry, Lund University, SE-22100 Lund, Sweden.

Langmuir : the ACS Journal of Surfaces and Colloids

|August 11, 2022

Summary

This summary is machine-generated.

Alpha-synuclein (aSyn) binding to lipid discs causes shape changes. Upon fibril formation, aSyn desorbs, returning discs to their original shape in an all-or-none process.

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Last Updated: Sep 1, 2025

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Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Millisecond Hydrogen/Deuterium-Exchange Mass Spectrometry for the Study of Alpha-Synuclein Structural Dynamics Under Physiological Conditions

Published on: June 23, 2022

Area of Science:

Biochemistry
Neuroscience
Biophysics

Background:

Alpha-synuclein (aSyn) is implicated in Parkinson's disease.
aSyn self-assembles into amyloid fibrils and interacts with lipid membranes.
Understanding aSyn-lipid interactions is crucial for synaptic function research.

Purpose of the Study:

To investigate the interaction of alpha-synuclein with model lipid bilayer discs.
To characterize the structural changes in lipid discs upon aSyn adsorption and desorption.

Main Methods:

Cryogenic transmission electron microscopy (cryo-TEM).
Small-angle neutron scattering (SANS).

Main Results:

aSyn adsorption induces a significant shape transition in lipid bilayer discs.
aSyn self-assembly into fibrils leads to desorption from the discs.
Desorption follows an all-or-none mechanism, resulting in binary coexistence of disc shapes.
Observed coexistence aligns with cooperative aSyn adsorption to anionic lipid bilayers.

Conclusions:

aSyn adsorption and fibril formation dynamically alter lipid membrane structure.
The all-or-none desorption mechanism highlights cooperative binding phenomena.
This study provides insights into the interplay between aSyn, lipids, and disease-associated aggregation.